Enzyme@bismuth-ellagic acid: a versatile platform for enzyme immobilization with enhanced acid-base stability

Junyang Xu, Guanhua Liu, Ying He, Liya Zhou, Li Ma, Yunting Liu, Xiaobing Zheng, Jing Gao, Yanjun Jiang

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Front. Chem. Sci. Eng. ›› 2023, Vol. 17 ›› Issue (6) : 784-794. DOI: 10.1007/s11705-022-2278-4
RESEARCH ARTICLE
RESEARCH ARTICLE

Enzyme@bismuth-ellagic acid: a versatile platform for enzyme immobilization with enhanced acid-base stability

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Abstract

In situ encapsulation is an effective way to synthesize enzyme@metal–organic framework biocatalysts; however, it is limited by the conditions of metal–organic framework synthesis and its acid-base stability. Herein, a biocatalytic platform with improved acid-base stability was constructed via a one-pot method using bismuth-ellagic acid as the carrier. Bismuth-ellagic acid is a green phenol-based metal–organic framework whose organic precursor is extracted from natural plants. After encapsulation, the stability, especially the acid-base stability, of amyloglucosidases@bismuth-ellagic acid was enhanced, which remained stable over a wide pH range (2–12) and achieved multiple recycling. By selecting a suitable buffer, bismuth-ellagic acid can encapsulate different types of enzymes and enable interactions between the encapsulated enzymes and cofactors, as well as between multiple enzymes. The green precursor, simple and convenient preparation process provided a versatile strategy for enzymes encapsulation.

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Keywords

bismuth-ellagic acid / in situ encapsulation / enzyme@MOF biocomposites

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Junyang Xu, Guanhua Liu, Ying He, Liya Zhou, Li Ma, Yunting Liu, Xiaobing Zheng, Jing Gao, Yanjun Jiang. Enzyme@bismuth-ellagic acid: a versatile platform for enzyme immobilization with enhanced acid-base stability. Front. Chem. Sci. Eng., 2023, 17(6): 784‒794 https://doi.org/10.1007/s11705-022-2278-4

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Acknowledgements

This work was financially supported by the National Natural Science Foundation of China (Grant Nos. 22178083, 22078081 and 21878068), the Natural Science Foundation of Tianjin China (Grant No. 20JCYBJC00530), the Hebei Key Research and Development Project (Grant No. 20372802D), Open Funding Project of the State Key Laboratory of Biocatalysis and Enzyme Engineering (Grant No. SKLBEE2020011), Science Technology Research Project of Higher Education of Hebei Province (Grant No. QN2021045) and Tianjin Enterprise Science and Technology Commissioner Project (Grant No. 21YDTPJC00810).

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Supplementary material is available in the online version of this article at https://dx.doi.org/10.1007/s11705-022-2278-4 and is accessible for authorized users.

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